CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001769
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Coagulation factor VIII 
Protein Synonyms/Alias
 Antihemophilic factor; AHF; Procoagulant component; Factor VIIIa heavy chain, 200 kDa isoform; Factor VIIIa heavy chain, 92 kDa isoform; Factor VIII B chain; Factor VIIIa light chain 
Gene Name
 F8 
Gene Synonyms/Alias
 F8C 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1281NDSTNRTKKHTAHFSacetylation[1]
1614EKTAFKKKDTILSLNacetylation[2]
Reference
 [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa. 
Sequence Annotation
 DOMAIN 20 348 F5/8 type A 1.
 DOMAIN 20 198 Plastocyanin-like 1.
 DOMAIN 206 348 Plastocyanin-like 2.
 DOMAIN 399 730 F5/8 type A 2.
 DOMAIN 399 573 Plastocyanin-like 3.
 DOMAIN 583 730 Plastocyanin-like 4.
 DOMAIN 1713 2040 F5/8 type A 3.
 DOMAIN 1713 1877 Plastocyanin-like 5.
 DOMAIN 1887 2040 Plastocyanin-like 6.
 DOMAIN 2040 2188 F5/8 type C 1.
 DOMAIN 2193 2345 F5/8 type C 2.
 REGION 760 1667 B.
 MOD_RES 365 365 Sulfotyrosine.
 MOD_RES 737 737 Sulfotyrosine.
 MOD_RES 738 738 Sulfotyrosine.
 MOD_RES 742 742 Sulfotyrosine.
 MOD_RES 1683 1683 Sulfotyrosine.
 MOD_RES 1699 1699 Sulfotyrosine.
 CARBOHYD 60 60 N-linked (GlcNAc...) (Potential).
 CARBOHYD 258 258 N-linked (GlcNAc...) (Potential).
 CARBOHYD 601 601 N-linked (GlcNAc...).
 CARBOHYD 776 776 N-linked (GlcNAc...) (Potential).
 CARBOHYD 803 803 N-linked (GlcNAc...) (Potential).
 CARBOHYD 847 847 N-linked (GlcNAc...) (Potential).
 CARBOHYD 919 919 N-linked (GlcNAc...) (Potential).
 CARBOHYD 962 962 N-linked (GlcNAc...) (Potential).
 CARBOHYD 982 982 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1020 1020 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1024 1024 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1074 1074 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1085 1085 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1204 1204 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1274 1274 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1278 1278 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1301 1301 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1319 1319 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1431 1431 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1461 1461 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1829 1829 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2137 2137 N-linked (GlcNAc...) (Potential).
 DISULFID 172 198
 DISULFID 267 348
 DISULFID 547 573
 DISULFID 649 730
 DISULFID 1851 1877
 DISULFID 1918 1922
 DISULFID 2040 2188
 DISULFID 2193 2345 By similarity.  
Keyword
 3D-structure; Acute phase; Alternative splicing; Blood coagulation; Calcium; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Hemophilia; Hemostasis; Metal-binding; Pharmaceutical; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Sulfation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2351 AA 
Protein Sequence
MQIELSTCFF LCLLRFCFSA TRRYYLGAVE LSWDYMQSDL GELPVDARFP PRVPKSFPFN 60
TSVVYKKTLF VEFTDHLFNI AKPRPPWMGL LGPTIQAEVY DTVVITLKNM ASHPVSLHAV 120
GVSYWKASEG AEYDDQTSQR EKEDDKVFPG GSHTYVWQVL KENGPMASDP LCLTYSYLSH 180
VDLVKDLNSG LIGALLVCRE GSLAKEKTQT LHKFILLFAV FDEGKSWHSE TKNSLMQDRD 240
AASARAWPKM HTVNGYVNRS LPGLIGCHRK SVYWHVIGMG TTPEVHSIFL EGHTFLVRNH 300
RQASLEISPI TFLTAQTLLM DLGQFLLFCH ISSHQHDGME AYVKVDSCPE EPQLRMKNNE 360
EAEDYDDDLT DSEMDVVRFD DDNSPSFIQI RSVAKKHPKT WVHYIAAEEE DWDYAPLVLA 420
PDDRSYKSQY LNNGPQRIGR KYKKVRFMAY TDETFKTREA IQHESGILGP LLYGEVGDTL 480
LIIFKNQASR PYNIYPHGIT DVRPLYSRRL PKGVKHLKDF PILPGEIFKY KWTVTVEDGP 540
TKSDPRCLTR YYSSFVNMER DLASGLIGPL LICYKESVDQ RGNQIMSDKR NVILFSVFDE 600
NRSWYLTENI QRFLPNPAGV QLEDPEFQAS NIMHSINGYV FDSLQLSVCL HEVAYWYILS 660
IGAQTDFLSV FFSGYTFKHK MVYEDTLTLF PFSGETVFMS MENPGLWILG CHNSDFRNRG 720
MTALLKVSSC DKNTGDYYED SYEDISAYLL SKNNAIEPRS FSQNSRHPST RQKQFNATTI 780
PENDIEKTDP WFAHRTPMPK IQNVSSSDLL MLLRQSPTPH GLSLSDLQEA KYETFSDDPS 840
PGAIDSNNSL SEMTHFRPQL HHSGDMVFTP ESGLQLRLNE KLGTTAATEL KKLDFKVSST 900
SNNLISTIPS DNLAAGTDNT SSLGPPSMPV HYDSQLDTTL FGKKSSPLTE SGGPLSLSEE 960
NNDSKLLESG LMNSQESSWG KNVSSTESGR LFKGKRAHGP ALLTKDNALF KVSISLLKTN 1020
KTSNNSATNR KTHIDGPSLL IENSPSVWQN ILESDTEFKK VTPLIHDRML MDKNATALRL 1080
NHMSNKTTSS KNMEMVQQKK EGPIPPDAQN PDMSFFKMLF LPESARWIQR THGKNSLNSG 1140
QGPSPKQLVS LGPEKSVEGQ NFLSEKNKVV VGKGEFTKDV GLKEMVFPSS RNLFLTNLDN 1200
LHENNTHNQE KKIQEEIEKK ETLIQENVVL PQIHTVTGTK NFMKNLFLLS TRQNVEGSYD 1260
GAYAPVLQDF RSLNDSTNRT KKHTAHFSKK GEEENLEGLG NQTKQIVEKY ACTTRISPNT 1320
SQQNFVTQRS KRALKQFRLP LEETELEKRI IVDDTSTQWS KNMKHLTPST LTQIDYNEKE 1380
KGAITQSPLS DCLTRSHSIP QANRSPLPIA KVSSFPSIRP IYLTRVLFQD NSSHLPAASY 1440
RKKDSGVQES SHFLQGAKKN NLSLAILTLE MTGDQREVGS LGTSATNSVT YKKVENTVLP 1500
KPDLPKTSGK VELLPKVHIY QKDLFPTETS NGSPGHLDLV EGSLLQGTEG AIKWNEANRP 1560
GKVPFLRVAT ESSAKTPSKL LDPLAWDNHY GTQIPKEEWK SQEKSPEKTA FKKKDTILSL 1620
NACESNHAIA AINEGQNKPE IEVTWAKQGR TERLCSQNPP VLKRHQREIT RTTLQSDQEE 1680
IDYDDTISVE MKKEDFDIYD EDENQSPRSF QKKTRHYFIA AVERLWDYGM SSSPHVLRNR 1740
AQSGSVPQFK KVVFQEFTDG SFTQPLYRGE LNEHLGLLGP YIRAEVEDNI MVTFRNQASR 1800
PYSFYSSLIS YEEDQRQGAE PRKNFVKPNE TKTYFWKVQH HMAPTKDEFD CKAWAYFSDV 1860
DLEKDVHSGL IGPLLVCHTN TLNPAHGRQV TVQEFALFFT IFDETKSWYF TENMERNCRA 1920
PCNIQMEDPT FKENYRFHAI NGYIMDTLPG LVMAQDQRIR WYLLSMGSNE NIHSIHFSGH 1980
VFTVRKKEEY KMALYNLYPG VFETVEMLPS KAGIWRVECL IGEHLHAGMS TLFLVYSNKC 2040
QTPLGMASGH IRDFQITASG QYGQWAPKLA RLHYSGSINA WSTKEPFSWI KVDLLAPMII 2100
HGIKTQGARQ KFSSLYISQF IIMYSLDGKK WQTYRGNSTG TLMVFFGNVD SSGIKHNIFN 2160
PPIIARYIRL HPTHYSIRST LRMELMGCDL NSCSMPLGME SKAISDAQIT ASSYFTNMFA 2220
TWSPSKARLH LQGRSNAWRP QVNNPKEWLQ VDFQKTMKVT GVTTQGVKSL LTSMYVKEFL 2280
ISSSQDGHQW TLFFQNGKVK VFQGNQDSFT PVVNSLDPPL LTRYLRIHPQ SWVHQIALRM 2340
EVLGCEAQDL Y 2351 
Gene Ontology
 GO:0005576; C:extracellular region; NAS:UniProtKB.
 GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
 GO:0005507; F:copper ion binding; IEA:InterPro.
 GO:0016491; F:oxidoreductase activity; IEA:InterPro.
 GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
 GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
 GO:0007155; P:cell adhesion; IEA:InterPro.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome. 
Interpro
 IPR000421; Coagulation_fac_5/8-C_type_dom.
 IPR001117; Cu-oxidase.
 IPR011706; Cu-oxidase_2.
 IPR011707; Cu-oxidase_3.
 IPR002355; Cu_oxidase_Cu_BS.
 IPR008972; Cupredoxin.
 IPR024715; Factor_5/8.
 IPR014707; Factor_8.
 IPR008979; Galactose-bd-like. 
Pfam
 PF00394; Cu-oxidase
 PF07731; Cu-oxidase_2
 PF07732; Cu-oxidase_3
 PF00754; F5_F8_type_C 
SMART
 SM00231; FA58C 
PROSITE
 PS01285; FA58C_1
 PS01286; FA58C_2
 PS50022; FA58C_3
 PS00079; MULTICOPPER_OXIDASE1 
PRINTS